41487-00-7

Usage

Uses

Used in Research and Laboratory Settings:
Z-ILE-VAL-OH is used as a research compound for studying protein synthesis, structure, and function. It helps scientists understand the interactions and behavior of proteins and enzymes within biological systems.
Used in Drug Development and Pharmaceuticals:
Z-ILE-VAL-OH is used as a peptide in the synthesis and modification of therapeutic peptides. Its potential applications in drug development and pharmaceuticals make it a valuable tool for creating new treatments and medications.

InChI:InChI=1/C19H28N2O5/c1-5-13(4)16(17(22)20-15(12(2)3)18(23)24)21-19(25)26-11-14-9-7-6-8-10-14/h6-10,12-13,15-16H,5,11H2,1-4H3,(H,20,22)(H,21,25)(H,23,24)

Upstream product

• 72-18-4 L-valine 
• 3391-99-9 N-Z-L-isoleucine N-hydroxysuccinimide ester 
• 53665-97-7 Z-Ile-ONB 
• 3160-59-6 N-Cbz-L-Isoleucine 
• 88962-27-0 Valin-2-bromethylester-hydrochlorid 
• 88962-38-3 N-Benzyloxycarbonyl-L-isoleucyl-L-valin-2-bromethylester 

Downstream Products

• 41017-96-3 L-isoleucyl-L-valine 
• 73809-01-5 Boc-GlyIleValGlu(OBut)Gln(Mbh)-OH 
• 94359-91-8 Z-Ile-Val-NHCH₂Ph 

Relevant academic research and scientific papers

Glycopeptide Synthesis: Selective C-terminal Deblocking and Peptide Chain Elongation of Glucosylserine Derivatives

Benzyloxycarbonyl-(Z-)serine 2-bromoethyl ester (3b) reacts with 2,3,4,6-tetra-O-benzoyl-α-D-glucopyranosyl bromide (14) to give the glucosylserine ester 15.After conversion into the corresponding 2-iodoethyl ester 23 the carboxylic group is deblocked selectively by reductive elimination using zinc.In this procedure the Z and the carbohydrate protective functions as well as the sensitive O-glycoside bond remain unaffected.The glycosylserine 24 is condensed with amino acid 2-bromoethyl esters 2 to form protected glycodipeptide 2-bromoethyl esters 18 which are extended to give glycotripeptide esters 25 after selective carboxyl deblocking.Whereas protected serine dipeptides 5 are glycosylated with 14 to form the conjugates 18, the glycosylation of the serine tripeptides 10 was not successful.

Studies of Bitter Peptides from Casein Hydrolyzate. II. Syntheses of Bitter Peptide Fragments and Analogs of BPIa (Arg-Gly-Pro-Pro-Phe-Ile-Val) from Casein Hydrolyzate

In order to investigate the relationship between bitterness and chemical structure of BPIa, eleven kinds of fragments and analogs of BPIa were synthesized. des-Gly2-BPIa and des-Pro4-BPIa exhibited extremely bitter taste. However, the pentapeptide (Arg-Gly-Pro-Pro-Phe) of BPIa possessed weak bitterness. The bitterness exhibition of BPIa probably derived from the spatial structure of its molecule.